1npi

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{{Seed}}
 
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[[Image:1npi.png|left|200px]]
 
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==Tityus Serrulatus Neurotoxin (Ts1) at atomic resolution==
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The line below this paragraph, containing "STRUCTURE_1npi", creates the "Structure Box" on the page.
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<StructureSection load='1npi' size='340' side='right'caption='[[1npi]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1npi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tityus_serrulatus Tityus serrulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NPI FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.16&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_1npi| PDB=1npi | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1npi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1npi OCA], [https://pdbe.org/1npi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1npi RCSB], [https://www.ebi.ac.uk/pdbsum/1npi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1npi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SCX1_TITSE SCX1_TITSE] Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. In addition, it stimulates the release of NO, IL-6 and TNF-alpha in J774.1 cells (PubMed:21549737). This toxin is active against both mammals and insects.<ref>PMID:21549737</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/np/1npi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1npi ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of the Ts1 toxin from the Brazilian scorpion Tityus serrulatus was investigated at atomic resolution using X-ray crystallography. Several positively charged niches exist on the Ts1 molecular surface, two of which were found to coordinate phosphate ions present in the crystallization solution. One phosphate ion is bound to the conserved basic Lys1 residue at the Ts1 N-terminus and to residue Asn49. The second ion was found to be caged by residues Lys12, Trp54 and Arg56. Lys12 and Tyr/Trp54 residues are strictly conserved in all classical scorpion beta-neurotoxins. The cavity formed by these residues may represent a special scaffold required for interaction between beta-neurotoxins and sodium channels. The charge distribution on the Ts1 surface and the results of earlier chemical modification studies and side-directed mutagenesis experiments strongly indicate that the phosphate-ion positions mark plausible binding sites to the Na(+) channel. The existence of two distinct binding sites on the Ts1 molecular surface provides an explanation for the competition between Ts1, depressant (LqhIT2) and excitatory (AaHIT) neurotoxins.
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===Tityus Serrulatus Neurotoxin (Ts1) at atomic resolution===
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Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with Na+ channels.,Pinheiro CB, Marangoni S, Toyama MH, Polikarpov I Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):405-15. Epub 2003, Feb 21. PMID:12595696<ref>PMID:12595696</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_12595696}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1npi" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12595696 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12595696}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1NPI is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Tityus_serrulatus Tityus serrulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPI OCA].
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==Reference==
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<ref group="xtra">PMID:12595696</ref><references group="xtra"/>
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[[Category: Tityus serrulatus]]
[[Category: Tityus serrulatus]]
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[[Category: Marangoni, S.]]
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[[Category: Marangoni S]]
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[[Category: Pinheiro, C B.]]
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[[Category: Pinheiro CB]]
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[[Category: Polikarpov, I.]]
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[[Category: Polikarpov I]]
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[[Category: Toyama, M H.]]
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[[Category: Toyama MH]]
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[[Category: Xcitatory neurotoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 15:14:01 2009''
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Current revision

Tityus Serrulatus Neurotoxin (Ts1) at atomic resolution

PDB ID 1npi

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